Proteomics

Dataset Information

0

Integrated lysine acetylation stoichiometry and proteomics analysis in human cells


ABSTRACT: Lysine acetylation is a widespread posttranslational modification that targets a large number of biological pathways. Recent studies reveal that lysine acetylation sites exhibit mainly low stoichiometry. Here we explored three sample preparation methods, the use of detergents for the chemical acetylation reaction in combination with stable and efficient alkylating reagent, to analyze the stoichiometry of acetylation in three human cell lines. We identified and determined the acetylation occupancy in about 1500 protein in each cell line. Lysine acetylation is highly dynamic, we determined variations in the acetylation stoichiometry when nearby residues are phosphorylated. The stoichiometric analysis in combination with quantitative proteomics allowed us to better understand the role of this PTM in different cells. We found that high abundance of the deacetylase SIRT1 correlates with less acetylation occupancy and abundance of ribosomes, proteins involved in ribosome biogenesis, rRNA processing, among others. We confirmed through the inhibition of SIRT1 with EX-527, followed by quantitative proteomics and acetylation stoichiometry analyzes, the negative role of this deacetylase on transcription and translation pathways. In addition, we found that SIRT1 positively regulates several metabolic pathways.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell

SUBMITTER: Jeovanis Gil  

LAB HEAD: Sergio Manuel Encarnación-Guevara

PROVIDER: PXD005903 | Pride | 2017-09-12

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
JV_140624_Qexactive_CF1.raw Raw
JV_140624_Qexactive_CF2.raw Raw
JV_140624_Qexactive_CF3.raw Raw
JV_140624_Qexactive_CG1.raw Raw
JV_140624_Qexactive_CG2.raw Raw
Items per page:
1 - 5 of 92
altmetric image

Publications

Lysine acetylation stoichiometry and proteomics analyses reveal pathways regulated by sirtuin 1 in human cells.

Gil Jeovanis J   Ramírez-Torres Alberto A   Chiappe Diego D   Luna-Peñaloza Juan J   Fernandez-Reyes Francis C FC   Arcos-Encarnación Bolivar B   Contreras Sandra S   Encarnación-Guevara Sergio S  

The Journal of biological chemistry 20170911 44


Lysine acetylation is a widespread posttranslational modification affecting many biological pathways. Recent studies indicate that acetylated lysine residues mainly exhibit low acetylation occupancy, but challenges in sample preparation and analysis make it difficult to confidently assign these numbers, limiting understanding of their biological significance. Here, we tested three common sample preparation methods to determine their suitability for assessing acetylation stoichiometry in three hu  ...[more]

Similar Datasets

2020-12-18 | PXD021986 | Pride
2017-11-09 | MSV000081704 | MassIVE
2019-03-12 | PXD009994 | Pride
2020-09-28 | PXD019268 | Pride
2016-03-01 | E-GEOD-75370 | biostudies-arrayexpress
2021-12-30 | PXD027173 | Pride
2016-10-05 | PXD000930 | Pride
2017-03-14 | PXD005720 | Pride
2007-09-28 | E-MEXP-1248 | biostudies-arrayexpress
2016-06-16 | PXD003611 | Pride